Please use this identifier to cite or link to this item: doi:10.22028/D291-30936
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Title: Reversible immobilization of a protein to a gold surface through multiple host-guest interactions
Author(s): Schwarz, Dennis H.
Elgaher, Walid A. M.
Hollemeyer, Klaus
Hirsch, Anna
Wenz, Gerhard
Language: English
Title: Journal of materials chemistry
Volume: 7
Issue: 40
Startpage: 6148
Endpage: 6155
Publisher/Platform: RSC
Year of Publication: 2019
Publikation type: Journal Article
Abstract: Monolayers were formed by specific interactions between adamantylated proteins (transferrin, lysozyme) and a β-cyclodextrin (β-CD) monolayer on a gold surface. Very high stabilities could be reached by multiple interactions of 3-6 adamantyl moieties linked through triethylene glycol spacers to the protein with β-CD rings attached to the surface. Furthermore, bound proteins could be completely removed from the surface through competitive binding of an excess of free adamantane. Regenerable protein sensor chips can be constructed by using this supramolecular toolbox. Attached proteins are still recognized by specific antibodies, which was attributed to a loose packing of the protein molecules at the β-CD monolayer.
DOI of the first publication: 10.1039/c9tb00560a
URL of the first publication:!divAbstract
Link to this record: hdl:20.500.11880/29150
ISSN: 2050-7518
Date of registration: 14-May-2020
Faculty: NT - Naturwissenschaftlich- Technische Fakultät
Department: NT - Pharmazie
Professorship: NT - Prof. Dr. Anna Hirsch
Collections:UniBib – Die Universitätsbibliographie

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